|専攻分野||structural biology, biochemistry|
I was born and grew up in Kyoto. In research, I am passionate and strict, but otherwise I am an open-minded and mild-mannered person. I am happiest when I can pioneer new research fields together with young people in Tohoku.
Kojima, R.†, Okumura, M.†, Masui, S., Kanemura, S., Inoue, M., Saiki, M., Yamaguchi, H., Hikima, T., Suzuki, M., Akiyama, S. and Inaba, K.* (†These authors contributed equally to this work.) “Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide-bond introducer of the mammalian PDI family”, Structure, 22, 431-443 (2014)
Sato, Y.†, Kojima, R.†, Okumura, M.†, Hagiwara, M.†, Masui, S., Maegawa, K., Saiki, M., Horibe, T., Suzuki, M. and Inaba, K.* (†These authors contributed equally to this work.) “Synergistic cooperation of PDI family member proteins in peroxiredoxin 4-driven oxidative protein folding” Scientific Reports 3, 2456 DOI: 10.1038 (2013)
Vavassori, S.†, Cortini, M.†, Masui, S.†, Sannino, S.†, Anelli, T., Caserta, I. R., Fagioli, C., Fornili, A., Mossuto, M. F., Degano, M, Inaba, K. and Sitia, R. (†These authors contributed equally to this work.) A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly. Mol. Cell 50, 783-792 (2013)
Hagiwara, M., Maegawa, K., Suzuki, M., Ushioda, R., Araki, K., Matsimoto, Y., Hoseki, J., Nagata, K.* and Inaba, K.* Structural basis of an ERAD pathway mediated by the ER-resident disulfide reductasse ERdj5. Mol. Cell 41, 432-444 (2011)
Masui, S., Vavassori, S., Fagioli, C., Sitia, R. and Inaba, K.* Molecular bases of cyclic and specific disulfide interchange between human Ero1α protein and protein-disulfide isomerase (PDI). J. Biol. Chem. 286, 16262-16271 (2011)
Inaba, K.*, Masui, S., Iida, H. Vavassori, S., Sitia, R. and Suzuki, M. Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J 29, 3330-3343 (2010)
Inaba, K.*, Murakami, S., Nakagawa, A., Iida, H., Kinjo, H., Ito, K. and Suzuki, M. Dynamic nature of disulfide bond formation catalysts revealed by crystal structures of DsbB. EMBO J 28, 779-791 (2009)
Inaba, K., Takahashi, Y. -H., Ito, K. and Hayashi, S. Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. Proc. Natl. Acad. Sci. USA. 103, 287-292 (2006)
Inaba, K.*, Murakami, S., Suzuki, M., Nakagawa, A., Yamashita, E., Okada, K. and Ito, K.* Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127, 789-801 (2006)
Protein Science Society of Japan, the Japanese Biochemical Society, the Molecular Biology Society of Japan, the Biophysical Society of Japan, Japan Society for Cell Biology
Advanced Lecture on Biomolecular Sciences, Advanced Biochemistry, Advanced Lecture on Metals Biology I
Disulfide bonds formed between two cysteine residues are known to play an important role in folding and functional regulation of proteins. Proteins endowed with disulfide bonds include immunoglobulins, MHC molecules, and defensin, which serve as the basis of the immune system; and hormones such as insulin and growth factor. We make full use of structural biology, biochemistry, proteomics, and cell biology techniques in the pursuit of thoroughly elucidating molecular mechanisms and new functional roles of disulfide bond formation and cleavage systems (networks) in cells. In particular, we have recently been conducting research focused on the protein quality control system in the endoplasmic reticulum of human cells. It has been widely reported that the failure of this system causes problems such as diabetes and neurodegenerative diseases like Alzheimer's and Parkinson's, and therefore I believe that our basic research is of much medical importance as well.
Do you hate to lose? Are you thinking about making a living through research? Are you interested in understanding biological phenomena at the molecular level? If you answer “yes” to all of the above, then let us research together. Achieving significant research results requires sense, insatiable enthusiasm, and just a little bit of luck. I am seeking tenacious individuals for my laboratory.